Effect of carbamination on the buffering power of purified human hemoglobin A solutions at two temperatures.
The effect of CO2 on hemoglobin buffering power was studied in purified human hemoglobin A solutions, native and specifically carbamoylated on N-terminal valines, at 26 degrees C and 42 degrees C, in the oxy and deoxy states. Titrations were performed by varying Pco2 and by strong acid or base in the absence of CO2. The participation of N-terminal valines to the total buffering power was estimated by subtracting the buffering value measured on carbamoylated hemoglobin solutions from that measured on native hemoglobin solutions. In the absence of CO2 the buffering value of native and modified hemoglobin increased slightly (less than 10%) (a) on going from the deoxy to the oxy state, and (b) on raising the temperature from 26 degrees C to 42 degrees C. In the presence of CO2 the buffering value of Hb increased from 9.1 to 16.6 mol mol Hb4-1 pH-1 and that of HbO2 from 10.1 to 19.6 mol mol Hb4-1 pH-1 when the temperature was raised from 26 degrees C to 42 degrees C. These figures correspond to a rise in the fraction of the total buffering value attributable to N-terminal valines from 11% to 25% for Hb and from 3% to 33% for HbO2. The present results point to a non-specific effect of CO2 within the hemoglobin molecule independent of that of N-terminal valines. This effect nearly doubles the buffering value for CO2 when the temperature is raised, and contributes to pH regulation and CO2 removal in tissues with a high metabolic rate.
D002021:Buffers; D002245:Carbon Dioxide / Q000494:pharmacology*; D006441:Hemoglobin A / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013696:Temperature
D002021:Buffers; D002245:Carbon Dioxide; D006441:Hemoglobin A